D- β-hydroxybutyrate dehydrogenase

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Mitochondrial β-hydroxybutyrate dehydrogenase
Properties of human protein
Mass / length primary structure 297 amino acids
Secondary to quaternary structure Homotetramer
Cofactor Phosphatidylcholine
Identifier
Gene names BDH1 SDR9C1
External IDs
Enzyme classification
EC, category 1.1.1.30 ,  oxidoreductase
Response type Oxidation or reduction
Substrate Acetoacetate + NADH / H +
Products D-β-hydroxybutyrate + NAD +
Occurrence
Parent taxon Mammals

D- β-hydroxybutyrate dehydrogenase ( BDH ) are called enzymes that catalyze the mutual conversion of acetoacetate into D- β-hydroxybutyrate and vice versa. This reaction equilibrium is necessary for the structure of the ketone body D- β-hydroxybutyrate in the liver of mammals and its breakdown in the tissue. Two paralogous isoforms are known ofBDH, BDH1 (coded on chromosome 3) is located in the mitochondria and BDH2 (coded on chromosome 4) in the cytosol .

BDH can also be found in some bacteria. It enables u. a. special Acidovorax and Ralstonia pickettii strains to break down the plastic polyhydroxybutyric acid . BDH can also be used to quickly measure the level of keto bodies in the blood.

The amino acid sequence of BDH is two-thirds identical to that of the short-chain alcohol dehydrogenases . If one looks at the structures, then it only differs in the substrate-binding domain and the phospholipid binding site.

Catalyzed equilibrium

Acetoacetate+ NADH / H + ⇔ Hydroxybutyrate+ NAD +

Acetoacetate and D- β-hydroxybutyrate merge. Phosphatidylcholine is required for the allosteric activation of the enzymatic activity of BDH .

Individual evidence

  1. ↑ UniProt Q02338 .
  2. ↑ BDH1 and BDH2
  3. ↑ Takanashi M, Shibahara T, Shiraki M, Saito T: Biochemical and genetic characterization of a D (-) - 3-hydroxybutyrate dehydrogenase from Acidovorax sp. strain SA1 . In: J. Biosci. Bioeng. . 97, No. 1, 2004, pp. 78-81. doi : 10.1016 / S1389-1723 (04) 70170-X . PMID 16233594 .
  4. ↑ Takanashi M, Saito T: Characterization of two 3-hydroxybutyrate dehydrogenases in poly (3-hydroxybutyrate) -degradable bacterium, Ralstonia pickettii T1 . In: J. Biosci. Bioeng. . 101, No. 6, June 2006, pp. 501-7. doi : 10.1263 / jbb.101.501 . PMID 16935252 .
  5. ↑ Laun RA, Rapsch B, Abel W, et al : The determination of ketone bodies: preanalytical, analytical and physiological considerations . In: Clin. Exp. Med. . 1, No. 4, December 2001, pp. 201-209. PMID 11918279 .
  6. ↑ D-β-hydroxybutyrate dehydrogenase.  In: Online Mendelian Inheritance in Man . (English).

Web links

Wikibooks: Biochemie_und_Pathobiochemie: ketone body biosynthesis  - learning and teaching materials